View source for 7jvg


==Cellular retinol-binding protein 2 (CRBP2) in complex with 1-arachidonoylglycerol==
<StructureSection load='7jvg' size='340' side='right'caption='[[7jvg]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7jvg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JVG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JVG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1AG:(2S)-2,3-DIHYDROXYPROPYL+(5Z,8Z,11Z,14Z)-ICOSA-5,8,11,14-TETRAENOATE'>1AG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7jvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jvg OCA], [https://pdbe.org/7jvg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jvg RCSB], [https://www.ebi.ac.uk/pdbsum/7jvg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jvg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RET2_HUMAN RET2_HUMAN] Intracellular transport of retinol.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Present in the small intestine, cellular retinol-binding protein 2 (CRBP2) plays an important role in the uptake, transport, and metabolism of dietary retinoids. However, the recent discovery of the interactions of CRBP2 with 2-arachidonoylglycerol (2-AG) and other monoacylglycerols (MAGs) suggests the broader involvement of this protein in lipid metabolism and signaling. To better understand the physiological role of CRBP2, we determined its protein-lipid interactome using a fluorescence-based retinol replacement assay adapted for a high-throughput screening format. By examining chemical libraries of bioactive lipids, we provided evidence for the selective interaction of CRBP2 with a subset of non-retinoid ligands with the highest affinity for sn-1 and sn-2 MAGs that contain polyunsaturated C18-C20 acyl chains. We also elucidated the structure-affinity relationship for non-retinoid ligands of this protein. We further dissect the molecular basis for this ligand's specificity by analyzing high-resolution crystal structures of CRBP2 in complex with selected derivatives of MAGs. Finally, we identify T51 and V61 as key amino acids that enable the broadening of ligand selectivity to MAGs in CRBP2 as compared to retinoid-specific CRBP1. Thus, our study provides the molecular framework for understanding the lipid selectivity and diverse functions of CRBPs in controlling lipid homeostasis.'

Molecular basis for the interaction of cellular retinol-binding protein 2 (CRBP2) with non-retinoid ligands.,Silvaroli JA, Plau J, Adams CH, Banerjee S, Widjaja-Adhi MAK, Blaner WS, Golczak M J Lipid Res. 2021 Feb 22:100054. doi: 10.1016/j.jlr.2021.100054. PMID:33631211<ref>PMID:33631211</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7jvg" style="background-color:#fffaf0;"></div>

==See Also==
*[[Retinol-binding protein 3D structures|Retinol-binding protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Golczak M]]
[[Category: Silvaroli JA]]